title: Controlling self-assembly of a peptide-based material via metal-ion induced registry shift.
abstract: Peptide TZ1C2 can populate two distinct orientations: a staggered (out-of-register) fibril and an aligned (in-register) coiled-coil trimer. The coordination of two cadmium ions induces a registry shift that results in a reversible transition between these structural forms. This process recapitulates the self-assembly mechanism of native protein fibrils in which a ligand binding event gates a reversible conformational transition between alternate forms of a folded peptide structure.
authors.affiliation: Department of Chemistry, Emory University, Atlanta, Georgia 30322, United States.
authors.forename: Paolo
authors.initials: P
authors.lastname: Anzini
authors.forename: Chunfu
authors.initials: C
authors.lastname: Xu
authors.forename: Spencer
authors.initials: S
authors.lastname: Hughes
authors.forename: Elizabeth
authors.initials: E
authors.lastname: Magnotti
authors.forename: Tao
authors.initials: T
authors.lastname: Jiang
authors.forename: Lars
authors.initials: L
authors.lastname: Hemmingsen
authors.forename: Borries
authors.initials: B
authors.lastname: Demeler
authors.forename: Vincent P
authors.initials: VP
authors.lastname: Conticello
mesh_terms: D002104:Cadmium / Q000737:chemistry*; D007477:Ions / Q000737:chemistry; D010316:Particle Size; D010455:Peptides / Q000737:chemistry*; D013499:Surface Properties
chemical_list: D007477:Ions; D010455:Peptides; D002104:Cadmium